• Korean Journal of Microbiology
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• v.22 no.2
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• pp.77-84
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• 1984

This examined some conditions for the induction of ${\beta}$-D-galactosidase synthesis in Candida kefyr CBS 834. The optimal pH, temperature, and inoculum size either for growth or${\beta}$-D-galactosidase synthesis were 5.5, $30^{\circ}C$ and above 0.2 at A610nm, respectively. Enzyme activity began to increase at 2h after the addition of inducer, and continued to increase linearly up to $2{\sim}3h$ before reaching stationary phase, and thereafter its activity was decreased. ${\beta}$-D-galactosidase was induced either by lactose or galactose but not either by glucose or ethanol. The greater activity of ${\beta}$-D-galactosidase on galactose than on lactose indicated that the former might be natural inducer for ${\beta}$-D-galactosidase synthesis. The rate of its induction as a function of lactose concentration showed that enzyme activity increased linearly above 4mM, while it was very low below that. Glucose represed the induction of ${\beta}$-D-galactosidase, and the period of adaptation to inducer from other carbon sources was relatively short.

• Journal of Ginseng Research
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• v.24 no.2
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• pp.89-93
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• 2000

WB were screening the stele and the cortex of the ginseng roots (Panax ginseng C.A.Meyer) on the exo-0-glycosylhydrolase activities during vegetation period of 1999 year. The following p-nitrophenylglycosides were used to test exe-0-glycosylhydrolase activities: $\alpha$- and $\beta$-D-galactopyranosides,$\alpha$- and $\beta$-D-glucopyranosides, $\alpha$- and $\beta$-D-mannopyranosides, N-acetyl-$\beta$-D-glucosaminide, $\alpha$- and $\beta$-D-xylopyranosides $\alpha$- L-rhamnopyranoside, $\beta$-D-glucuronide, $\beta$-D-galacturonide, $\beta$-L-,$\alpha$-L- and $\beta$-D-fucopyranosides, $\alpha$-L-arabinopyranoside. Only $\beta$-D-galactosidase, $\alpha$-L-mannosi-dase , N- acetyl- ${\beta}$-D-slucosarninidase, $\alpha$-D-galacto sidase, $\alpha$-L-arabinosidase, and $\beta$-D-fuco sidase were found in both partsof ginseng roots. Their contents during the vegetation period were shown to differ considerably, being dependent not only on plant development stage but on plant tissue and environmental conditions too.

• Journal of Applied Biological Chemistry
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• v.43 no.3
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• pp.141-146
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• 2000

Glycosidase activities were tested from the grape berries, Vitis labruscana B. Takasumi. Among various glycosidases, $\alpha$-D-galactosidase was found to be the most active in the flesh and other glycosidases were considerably active in the order of the following: $\alpha$-D-mannosidase>$\alpha$-D-glucosidase>$\beta$-D-glucosidase>$\beta$-D-galactosidase. In the seeds, $\alpha$-D-glucosidase activity was the highest and other glycosidases such as $\alpha$-D-galactosidase, $\beta$-D-glucosidase, and $\beta$-D-galactosidase were still significantly active. The $\alpha$-D-galactosidase in the grape flesh was purified over 83-folds through salting-out with $(NH_4)_2SO_4$ and a series of chromatographies employing Sephadex G-50, Octyl-Sepharose, Q-Sepha- rose, and Biogel P-100. The enzyme was a monomer of 45 kDs as determined through SDS-PAGE and Sephacryl S-200 chromatography. The purified enzyme showed a preference of $\alpha$-D-galactose to $\beta$-D-galactose as a substrate about 5.4 times. Sulfhydryl specific reagents such as N-ethylmaleimide and iodoacetamide significantly inhibited the enzyme activity to the extents of 48 and 52% of its initial activity, respectively. The optimumpH range of $\alpha$-D-galactosidase was around 6.5-7.0. The enzyme activity increased by 46% in the presence of 1mM $Fe^{2+}$.

• Journal of Microbiology and Biotechnology
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• v.18 no.3
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• pp.434-442
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• 2008

We observed that an inclusion body (IB) of recombinant ${\beta}$-galactosidase that was produced by the araBAD promoter system in Escherichia coli (E. coil) showed enzyme activity. In order to improve its activity, the lowering of the transcription rate of the ${\beta}$-galactosidase structural gene was attempted through competition between an inducer (L-arabinose) and an inducer analog (D-fucose). In the deep-well microtiter plate culture and lab-scale fermentor culture, it was demonstrated that the addition of D-fucose caused an improvement in specific ${\beta}$-galactosidase production, although ${\beta}$-galactosidase was produced as an IB. In particular, the addition of D-fucose after induction led to an increase in the specific activity of ${\beta}$-galactosidase IB. Finally, we confirmed that the addition of D-fucose after induction caused changes in the structure of ${\beta}$-galactosidase IB, with higher enzyme activity. Based on these results, we expect that an improved enzyme IB will be used as a biocatalyst of the enzyme bioprocess, because an enzyme IB can be purified easily and has physical durability.

• Microbiology and Biotechnology Letters
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• v.31 no.2
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• pp.151-156
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• 2003

A strain YB-10 was isolated from soil as a producer of the extracellular $\beta$-D-galactosidase, which catalyzes the hydrolysis of lactose. The strain YB-10 was identified as Streptomyces sp. on the basis of its cultural, morphological and physiological properties. After treating culture supernatant of the isolate with ammonium sulfate, the precipitated protein was used as a crude $\beta$-galactosidase for analyzing its reaction properties with para-nitrophenyl-$\beta$-D-galactosidase(pNP-$\beta$Gal) as a substrate. The $\beta$-galactosidase showed its maximal activity at pH 6.0 and 6$0^{\circ}C$. The enzyme was also active on lactose. The hydrolyzing activity of $\beta$-galactosldase for pNP-$\beta$Gal and lactose was decreased by galactose. Its hydrolyzing activity far lactose was also decreased by glucose, but the activity for pNP-$\beta$Gal was increased to 1.8-folds by glucose.

• Microbiology and Biotechnology Letters
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• v.20 no.1
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• pp.46-52
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• 1992

The optimum condition for the developement of a whey beverage from the concentrated whey was studied. Reverse osmosis system was used to obtain concentrated lactose from cheese whey. The hydrolysis degree of lactose by $\beta$-D-galactosidase was determined using HPLC (high performance liquid chromatography). The order of hydrolysis degree was 1:1, 2:l and 3:l concentrated lactose. It resulted from the concentrated salt which slightly inhibited $\beta$-D-galactosidase with constant enzyme dosage. The optimum condition for enzyme dosage was 2% in non-concentrated lactose, 3% in 2:l and 3% in 3:l concentrated lactose after 4 hours of reaction. When the 3:l concentrated lactose was used, more than 70% was hydrolyzed by 3% enzyme dosage. Furthermore the change of fermented whey by lactic acid bacteria was investigated. Based on the result of sensory test, the most favorable response was obtained at pH 4.2 and titratable acidity of 0.7% about 6 hours of fermentation at $37^{\circ}C$ with 2%: thermophilic starter.

• Microbiology and Biotechnology Letters
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• v.42 no.4
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• pp.339-346
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• 2014

A bacterial strain was isolated from homemade doenjang (Korean fermented soybean paste) as a producer of the extracellular ${\beta}$-galactosidase, capable of hydrolyzing lactose to liberate galactose and glucose residues. The isolate YB-1414 has been identified as Bacillus licheniformis on the basis of its 16S rDNA sequence, morphology and biochemical properties. The production of ${\beta}$-galactosidase by B. licheniformis YB-1414 reached maximum levels of 6.2 U/ml in culture medium containing wheat bran (1%) and yeast extract (2.5%) as carbon and nitrogen sources, respectively. Particularly, the insoluble fraction was more effective for ${\beta}$-galactosidase production than the soluble extract of wheat bran. The enzyme exhibited maximum activity for hydrolysis of para-nitrophenyl-${\beta}$-D-galactopyranoside (pNP-${\beta}Gal$) under reaction conditions of pH 6.0 and $55-60^{\circ}C$. Its hydrolyzing activity for pNP-${\beta}Gal$ was drastically decreased by the addition of low concentrations of galactose, but only slightly decreased by glucose, with 85% of maximal activity in the presence of 400 mM glucose.

• Korean Journal of Food Science and Technology
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• v.21 no.1
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• pp.164-172
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• 1989

The formation of galactooligosaccharides by transgalactosidation reactions during hydrolysis of lactose by the ${\beta}-galactosidase$ from Streptococcus thermophilus 510 was investigated. Three oligosaccharides were detected during hydrolysis. It was found that the optimum conditions for the production of oligosaccharides was 40% lactose treated with ${\beta}-galactosidase(50\;ONPG\;units/ml)$ at $37^{\circ}C$ for 4 hours. The oligosaccharides formed accounted for 30% of the total sugars when the lactose had been 94% hydrolysed. 69% of the oligosaccharides were identified as $6-o-{\beta}-D-galactopyranosyl-D-glucose(allolactose)$ and 23% as $6-o-{\beta}-D-galactopyranosyl-D-galactose(isogalactobiose)$. The separation of galactooligosaccharides by the use of Bio-Gel P-2 gel permeation chromatography was also studied.

• Microbiology and Biotechnology Letters
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• v.18 no.6
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• pp.566-570
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• 1990

Regulation of $\beta$ -galactosidase formation was studied with Lactobacillus sporogenes. Synthesis of the enzyme was effectively induced by isopropyl- $\beta$-D-thiogalactopyranoside (IPTG) or galactose, and to a much lower level by lactose. When 15 mM glucose was added at the different intervals to the cultures that had been in contact with IPTG, the same levels of inhibition of the enzyme synthesis were observed (approximately one-third the differential rate of a control culture without glucose). This suggests that glucose did not interfere with the entry of the inducer into the cells, but interfere with the formation of $\beta$ -galactosidase through catabolite repression. The glucose inhibitory effect was not overcome by adding CAMP or cGMP to the culture media.

• The Journal of Natural Sciences
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• v.4
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• pp.59-68
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• 1991

$\beta$-Galactosidase(EC 3.2.1.23) from pathogenic Neisseria lactamica 2118 was purified by p-aminopheny1-$\beta$-D-thiogalactopyranoside agarose affinity chromatography. Then some properties of the purified $\beta$-galactosidase were investigated.$\beta$-Galactosidase form Neisseria lactamica 2118 was constitutive enzyme, not induced by lactose and IPTG. Optimal activity was observed at $35^{\circ}C$ and pH 7.5 and the enzyme was stable at the range of pH 6.0-9.0 and at temperature below $50^{\circ}C$. The enzyme activity was inhibited by cations such as $Hg^(2+)$ and $Co^(2+)$.